1ccn
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ccm|1CCM]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ccn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ccn OCA], [http://www.ebi.ac.uk/pdbsum/1ccn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ccn RCSB]</span> | ||
}} | }} | ||
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[[Category: plant seed protein]] | [[Category: plant seed protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:19:13 2008'' |
Revision as of 16:19, 30 March 2008
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| Related: | 1CCM
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DIRECT NOE REFINEMENT OF CRAMBIN FROM 2D NMR DATA USING A SLOW-COOLING ANNEALING PROTOCOL
Overview
A set of computer programs called DINOSAUR has been developed, which allows the refinement of biomolecular structures directly from 2D NOE intensities. The NOE restraining potential implemented emphasises the weak intensities corresponding to larger distances which are more likely to determine the three-dimensional structure. An approximation based on a two-spin approximation is proposed for the gradient of the NOE intensities instead of the exact solution which is extremely time-consuming. The DINOSAUR routines have been implemented in various refinement programs (Distance bound Driven Dynamics, Molecular Dynamics and Energy Minimisation) and tested on an eight-residue model peptide.
About this Structure
1CCN is a Single protein structure of sequence from Crambe hispanica subsp. abyssinica. Full crystallographic information is available from OCA.
Reference
Direct NOE refinement of biomolecular structures using 2D NMR data., Bonvin AM, Boelens R, Kaptein R, J Biomol NMR. 1991 Sep;1(3):305-9. PMID:1841701
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